Sandbox WWC1: Difference between revisions
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== Structure == | == Structure == | ||
BTX is produced as a single chain protein in the bacterium, but becomes active when a protease cuts the protein into a heavy and light chain connected by a single disulfide bong. The heavy chain is approximately 100 kDa and the light chain is 50 kDa. | BTX is produced as a single chain protein in the bacterium, but becomes active when a protease cuts the protein into a heavy and light chain connected by a single disulfide bong. The heavy chain is approximately 100 kDa and the light chain is 50 kDa (for reviews about structure see references <ref>Sakaguchi G. 1983. Clostridium botulinum toxins. Pharmacol. Ther. 19:165– | ||
94. </ref> <ref> Minton NP. 1995. Molecular genetics of | |||
clostridial neurotoxins. Curr. Top. Microbiol. | |||
Immunol. 195:161–94 </ref> <ref> Oguma K, Fujinaga Y, Inoue K. 1995.Structure and function of Clostridium botulinum toxins. Microbiol. Immunol. 39:161–68 </ref> <ref> Lacy BD, Stevens RC. 1999. Sequence homology and structural analysis of the clostridial neurotoxins. J. Mol. Biol. 291: 1091–104 </ref> <ref> Popoff MR, Marvaud J-C. 1999. Structural and genomic features of clostridial neurotoxins. See Ref. 132, pp. 174– | |||
201 </ref>. | |||
The light chain contains the consensus sequence HELIH that codes for the binding of zinc, which subsequently regulates the endopeptidase activity of the light chain. | The light chain contains the consensus sequence HELIH that codes for the binding of zinc, which subsequently regulates the endopeptidase activity of the light chain. | ||
BTX also has two | BTX also has two auxiliary proteins that compromise a multimeric complex: hemagglutinins (HA) and nonhemagglutinin (NTNH). HA and NTNH do not directly play a role in the toxic effect of BTX, but have an indirect role during ingestion of the protein by making the BTX more resistant to low pH environments and proteolytic enzymes found in the gut. | ||
== Function == | == Function == | ||